Protein increasing cell infectivity of herpes simplex virus and use thereof
a technology cell infectivity, which is applied in the direction of viruses, peptide/protein ingredients, fusion polypeptides, etc., can solve the problems of weak immunoreactivity, low transduction efficiency of hsv, and limited gene size, so as to increase the cell infectivity of herpes simplex virus
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example 1
HSV Infection by sHveA82 and sHveA107
[0058]It was identified whether protein efficiently mediates the entry of a virus into HSV-resistant cells, CHO-K1 cells in the same manner as in Comparative Example 3, except that recombinant sHveA82 protein and recombinant sHveA107 protein were used. In FIG. 7A, the x-axis indicates 500 nM recombinant sHveA proteins, and the number on the y-axis indicates the level of the virus infection. FIG. 7B illustrates infected cells according to the increasing concentrations of sHveA protein.
example 2
Preparation of Recombinant Expression Vector Expressing Anti-CEA scFv-HA82
[0059]An anti-CEA scFv gene was obtained by PCR using a forward primer (SEQ ID NO: 7) and a reverse primer (SEQ ID NO: 8), and using a pre-provided anti-CEA scFv gene as a template. The PCR was performed as follows: 0.1 μg of anti-CEA scFv DNA, 10 pmol of primers (SEQ ID NOS: 7 and 8, respectively), 10 units of Taq polymerase (Takara), 1× buffer solution, and 2.5 mM dNTP were mixed and water was added thereto such that the volume of the mixture was 50 μl. The anti-CEA scFv DNA was amplified by pre-denaturing the template DNA at 95° C. for 5 minutes, performing 30 cycles: at 94° C. for 1 minute, at 60° C. for 1 minute, and at 72° C. for 1 minute, and performing a final extension at 72° C. for 10 minutes. The amplified anti-CEA scFv DNA was isolated using column chromatography. The reverse primer (SEQ ID NO: 8) included a base sequence encoding GGGGS amino acid sequence (SEQ ID NO: 19). In order to insert the a...
example 3
Expression and Purification of Recombinant Anti-CEA scFv-HA82 Protein
[0061]Expression and purification of the recombinant anti-CEA scFv-HA82 protein were performed in the same manner as in Comparative Example 2. As shown in FIG. 4, protein having about 37 kDa of molecular size (lane 2) was isolated and purified.
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